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    Immunity. 1996 Mar;4(3):203-13.

    An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501.

    Smith KJ, Reid SW, Stuart DI, McMichael AJ, Jones EY, Bell JI.

    Nuffield Department of Clinical Medicine, Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, United Kingdom.

    The crystal structure of the human major histocompatibility complex class I B allele HLA B*3501 complexed with the 8-mer peptide epitope HIV1 Nef 75-82 (VPLRPMTY) has been determined at 2.0 angstrom resolution. Comparison with the crystal structure of the closely related allele HLA B*5301 reveals the structural basis for the tyrosine specificity of the B*3501 F pocket. The structure also reveals a novel conformation of the 8-mer peptide within the binding groove. The positions of the peptide N and C termini are nonstandard, but the classic pattern of hydrogen bonding to nonpolymorphic MHC class I residues is maintained, at the N terminus by addition of a water molecule, and at the C terminus by a substantial shift in the alpha 2 helix.

    PMID: 8624811 [PubMed - indexed for MEDLINE]

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